5GRR

Crystal structure of MCR-1

Summary for 5GRR

• Entry DOI: 10.2210/pdb5grr/pdb
• Descriptor: Probable phosphatidylethanolamine transferase Mcr-1, ZINC ION, GLYCEROL, ... (4 entities in total)
• Functional Keywords: antibiotic resistant, colistin, superbug, phosphoenthanolamine transferase, mcr-1, transferase
• Biological source: Escherichia coli
• Cellular location: Cell inner membrane ; Multi-pass membrane protein : A0A0R6L508
• Total number of polymer chains: 1
• Total formula weight: 36560.88

Authors

Ma, G.,Zhu, Y.,Yu, Z.,Zhang, H. (deposition date: 2016-08-12, release date: 2017-01-04, Last modification date: 2024-11-13)

Primary citation

Ma, G.,Zhu, Y.,Yu, Z.,Ahmad, A.,Zhang, H.
High resolution crystal structure of the catalytic domain of MCR-1
Sci Rep, 6:39540-39540, 2016

PubMed Abstract: The newly identified mobile colistin resistant gene (mcr-1) rapidly spread among different bacterial strains and confers colistin resistance to its host, which has become a global concern. Based on sequence alignment, MCR-1 should be a phosphoethanolamine transferase, members of the YhjW/YjdB/YijP superfamily and catalyze the addition of phosphoethanolamine to lipid A, which needs to be validated experimentally. Here we report the first high-resolution crystal structure of the C-terminal catalytic domain of MCR-1 (MCR-1C) in its native state. The active pocket of native MCR-1C depicts unphosphorylated nucleophilic residue Thr285 in coordination with two Zinc ions and water molecules. A flexible adjacent active site loop (aa: Lys348-365) pose an open conformation compared to its structural homologues, suggesting of an open substrate entry channel. Taken together, this structure sets ground for further study of substrate binding and MCR-1 catalytic mechanism in development of potential therapeutic agents.

PubMed: 28000749
DOI: 10.1038/srep39540

Experimental method

X-RAY DIFFRACTION (1.45 Å)